Native mass spectrometry (MS) involves the analysis and characterization of
macromolecules, predominantly intact proteins and protein complexes, whereby as much as …

Native mass spectrometry (nMS) is evolving into a workhorse for structural biology. The
plethora of online and offline preparation, separation, and purification methods as well as …

Salts are often necessary to maintain the native structures and functions of many proteins
and protein complexes, but many buffers adversely affect protein analysis by native mass …

Mass spectrometry (MS) is increasingly being used to probe the structure and dynamics of
proteins and the complexes they form with other macromolecules. There are now several …

Ion mobility-mass spectrometry (IM-MS) can be a powerful tool for determining structural
information about ions in the gas phase, from small covalent analytes to large, native-like or …

Membrane proteins are embedded in the biological membrane where the chemically
diverse lipid environment can modulate their structure and function. However, the …

Electrospray ionization (ESI) mass spectrometry (MS) is a crucial method for rapidly
determining the interactions between small molecules and proteins with ultrahigh sensitivity …

Nonvolatile salts are essential for the structures and functions of many proteins and protein
complexes but can severely degrade performance of native mass spectrometry by adducting …

The study of drug–protein interactions can reveal the corresponding binding mechanisms,
providing valuable information for the early phase drug development and development of …

Over the past decades, substantial advances have been made in both the early diagnosis
and accurate prognosis of many cancers because of the impressive development of novel …